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Literature summary extracted from

  • Bianco, A.; Reghellin, V.; Donnici, L.; Fenu, S.; Alvarez, R.; Baruffa, C.; Peri, F.; Pagani, M.; Abrignani, S.; Neddermann, P.; De Francesco, R.
    Metabolism of phosphatidylinositol 4-kinase IIIalpha-dependent PI4P is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activity (2012), PLoS Pathog., 8, e1002576.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.67 isolated catalytic domain of isozyme PI4KIIIalpha as His-tagged protein in Spodoptera frugiperda Sf9 cells via transfection by recombinant baculovirus Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.67 [5-(4-[[4-(morpholin-4-yl)phenyl]amino]quinazolin-6-yl)furan-2-yl]methanol i.e. AL-9, a 4-anilino quinazoline, inhibits purified PI4KIIIalpha and, to a lesser extent, PI4KIIIbeta, and inhibits PI4KIIIalpha in vivo Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.67 Golgi membrane isozyme PI4KIIIbeta Homo sapiens 139
-
2.7.1.67 plasma membrane isozyme PI4KIIIalpha Homo sapiens 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.67 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.67 ATP + 1-phosphatidyl-1D-myo-inositol Homo sapiens
-
 ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.67 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.67 recombinant His-tagged catalytic domain of isozyme PI4KIIIalpha from Sf9 cells by nickel affinity chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.67 Huh-7.5 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.67 ATP + 1-phosphatidyl-1D-myo-inositol
-
 Homo sapiens ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.67 PI4KIIIalpha
-
 Homo sapiens
2.7.1.67 PI4KIIIbeta
-
 Homo sapiens
2.7.1.67 type III phosphatidylinositol 4-kinase alpha
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.67 22
-
 assay at room temperature Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.67 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.67 ATP
-
 Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.1.67 0.00057
-
 isozyme PI4KIIIalpha, pH 7.5, 22°C Homo sapiens [5-(4-[[4-(morpholin-4-yl)phenyl]amino]quinazolin-6-yl)furan-2-yl]methanol
2.7.1.67 0.0031
-
 isozyme PI4KIIIbeta, pH 7.5, 22°C Homo sapiens [5-(4-[[4-(morpholin-4-yl)phenyl]amino]quinazolin-6-yl)furan-2-yl]methanol

General Information

EC Number General Information Comment Organism
2.7.1.67 malfunction hepatitis C virus, by recruiting PI4KIIIa in the RNA replication complex, hijacks phosphatidylinositol-4 phosphate metabolism, ultimately resulting in a markedly altered subcellular distribution of the PI4KIIIalpha product. Antiviral effect of 4-anilino quinazoline compounds is mediated by the inhibition of PI4KIIIalpha and the consequent depletion of 1-phosphatidyl-1D-myo-inositol 4-phosphate required for the HCV membranous web. Inhibition of PI4KIIIalpha by AL-9 induces the formation of large viral NS5A protein clusters Homo sapiens
2.7.1.67 physiological function PI4KIIIalpha is responsible for the phosphatidylinositol-4 phosphate pool present in the plasma membrane. Antiviral effect of 4-anilino quinazoline compounds is mediated by the inhibition of PI4KIIIalpha and the consequent depletion of 1-phosphatidyl-1D-myo-inositol 4-phosphate required for the HCV membranous web Homo sapiens